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Literature summary extracted from

  • Christian, E.L.; Kaye, N.M.; Harris, M.E.
    Evidence for a polynuclear metal ion binding site in the catalytic domain of ribonuclease P RNA (2002), EMBO J., 21, 2253-2262.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.1.26.5 additional information the use of Ca2+ as catalytic metal ion is enhanced in nucleotide point mutants C70U and U69 deletion in the P4 helix Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.26.5 phosphorothionate modifies nucleotides A67Rp and A67Sp, no remaining activity with Mg2+, complete rescue of activity with 5 mM Mn2+ for A67Rp, partially 65fold for A67Sp Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.26.5 Mg2+ coordination to nucleotide A67 of the enzymes RNA Escherichia coli
3.1.26.5 Mn2+ rescues A67Rp- and A67Sp-phosphorothionate modified inactive enzyme at 5 mM completely and partially, respectively Escherichia coli
3.1.26.5 additional information at least 2 metal ions per enzyme molecule, one catalytically and one structurally important, interactions of divalent metal cations at the pro-Rp and ProSp non-bridging phosphate oxygens with nucleotide A67 in the universally conserved helix p4 are essential for the folding and function of the enzymes' catalytic RNA component, interaction kinetics Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.5 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.26.5 endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor an RNA-containing enzyme, essential for tRNA processing, generates 5'-termini or mature tRNA molecules, secondary structural features, e.g. helix P4, sequence J5/15 or J18/2 in the RNA portion of the enzyme, are important for catalysis Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.5 tRNA precursor + H2O cleavage of 5'-terminal oligonucleotide Escherichia coli mature tRNA + 5'-oligonucleotide generates 5'-phosphate,3'-hydroxyl-product ?

Subunits

EC Number Subunits Comment Organism
3.1.26.5 More enzyme folding and function are dependent on divalent metal cations, clustered interactions, e.g. with the helix P4 of the enzymes' RNA part, secondary structure of the RNA moiety, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.1.26.5 RNase P RNA
-
 Escherichia coli
3.1.26.5 tRNA processing enzyme
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.26.5 50
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.26.5 5.5
-
 assay at Escherichia coli